{"title":"基于酵母鸟嘌呤核苷酸结合蛋白γ亚基膜募集的受体和酶的功能分析和亲和改变","authors":"Nobuo Fukuda, S. Honda","doi":"10.14800/RCI.373","DOIUrl":null,"url":null,"abstract":"To investigate fundamental processes conserved in all eukaryotic cells, the budding yeast Saccharomyces cerevisiae has being widely used as a model organism. In particular, the yeast two-hybrid system is a powerful technique for analyzing protein–protein interactions and protein function in living cells. Here, we describe several approaches for investigating and regulating the activity of target proteins using the yeast guanine nucleotide-binding protein (G-protein) signaling machinery as the readout. These approaches are rapid and easy-to-use tools that support the design of regulatory factors against receptors, enzymes, and other proteins that have been identified as potential drug target molecules.","PeriodicalId":20980,"journal":{"name":"Receptors and clinical investigation","volume":"1 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2014-11-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Functional analyses and affinity-alteration of receptors and enzymes based on membrane recruitment of yeast guanine nucleotide-binding protein gamma subunit\",\"authors\":\"Nobuo Fukuda, S. Honda\",\"doi\":\"10.14800/RCI.373\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"To investigate fundamental processes conserved in all eukaryotic cells, the budding yeast Saccharomyces cerevisiae has being widely used as a model organism. In particular, the yeast two-hybrid system is a powerful technique for analyzing protein–protein interactions and protein function in living cells. Here, we describe several approaches for investigating and regulating the activity of target proteins using the yeast guanine nucleotide-binding protein (G-protein) signaling machinery as the readout. These approaches are rapid and easy-to-use tools that support the design of regulatory factors against receptors, enzymes, and other proteins that have been identified as potential drug target molecules.\",\"PeriodicalId\":20980,\"journal\":{\"name\":\"Receptors and clinical investigation\",\"volume\":\"1 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2014-11-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Receptors and clinical investigation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.14800/RCI.373\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Receptors and clinical investigation","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.14800/RCI.373","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Functional analyses and affinity-alteration of receptors and enzymes based on membrane recruitment of yeast guanine nucleotide-binding protein gamma subunit
To investigate fundamental processes conserved in all eukaryotic cells, the budding yeast Saccharomyces cerevisiae has being widely used as a model organism. In particular, the yeast two-hybrid system is a powerful technique for analyzing protein–protein interactions and protein function in living cells. Here, we describe several approaches for investigating and regulating the activity of target proteins using the yeast guanine nucleotide-binding protein (G-protein) signaling machinery as the readout. These approaches are rapid and easy-to-use tools that support the design of regulatory factors against receptors, enzymes, and other proteins that have been identified as potential drug target molecules.